NR AWLJ
AU Ollesch,J.; Künnemann,E.; Glockshuber,R.; Gerwert,K.
TI alpha-beta-transition of full-length prion protein monitored with timeresolved FTIR
QU International Conference - Prion 2006: Strategies, advances and trends towards protection of society - 3.10.-6.10.2006, Torino, Italy, Lingotto Conference Centre - Poster sessions
PT Konferenz-Poster
AB
FTIR-spectroscopy is a versatile tool to examine the secondary structure of a protein. Typically, the amide I band (C=O-stretching vibration of the backbone) is analysed by fitting Lorentz- and Gauss-shaped curves to its shape. We present the application of an improved approach to cope with the general experimental underdetermination of this method to the time resolved refolding reaction of re. mPrP(23-231).
We analyzed the kinetics of the folding reaction, finding a transient intermediate. Further characterization of the secondary structure distribution in the three relevant states displayed the folding reaction passing a partially unfolded intermediate with structurally conserved cooperative folding units. We achieved an estimated low error, determined with the deviation from NMR sturctural data from the ground state. We further present a newly developed mixing device, a microchip etched on a silicon wafer. The dead time of continuous-flo-mixing could thus be reduced down to 400 µsec.
AD J. Ollesch, K. Gerwert: Lehrstuhl für Biophysik, Ruhr-Universität Bochum, 44780 Bochum, Germany, http://www.bph.rub.de; ollesch@bph.rub.de, gerwert@bph.ruhr-uni-bochum.de; E. Künnemann, R. Glockshuber: Institut für Molekularbiologie und Biophysik, ETH Hönggerberg, CH-8093 Zürich, Switzerland
SP englisch
PO Italien